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User:Marie-Line Garron

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After a Ph.D. obtained in 2007 from the University of Montpellier (France), I joined Mirek Cygler's group, as postdoctoral student, at the Biotechnological Reasearch Institut (Montreal, QC, Canada). My postdoctoral research focused on the structure and function of CAZymes involved in synthesis and degradation of glycosaminoglycans (GAGs), and in particular on Polysaccharide Lyases on which I wrote two reviews.

In 2010, I joined the glycogenomic group, led by Bernard Henrissat at AFMB laboratory (Marseille, France), as postdoctoral researcher in charge of strengthening the functional and structural side of the team. I then obtained a permanent position as Assistant Professor in Aix-Marseille University in 2011.

I currently manage the updates of structural and functional information in the CAZy database. My personal research interests are with the biochemical and structural characterization of distant members of CAZy families and with the discovery of new CAZymes families.


Reviews

  1. Garron ML and Henrissat B. (2019) The continuing expansion of CAZymes and their families. Curr Opin Chem Biol. 53, 82-87. DOI:10.1016/j.cbpa.2019.08.004 | PubMed ID:31550558 | HubMed [Garron2019]
  2. Garron ML and Cygler M. (2014) Uronic polysaccharide degrading enzymes. Curr Opin Struct Biol. 28, 87-95. DOI:10.1016/j.sbi.2014.07.012 | PubMed ID:25156747 | HubMed [Garron2014]
  3. Garron ML and Cygler M. (2010) Structural and mechanistic classification of uronic acid-containing polysaccharide lyases. Glycobiology. 20, 1547-73. DOI:10.1093/glycob/cwq122 | PubMed ID:20805221 | HubMed [Garron2010]
All Medline abstracts: PubMed | HubMed

Publications

  1. Turbe-Doan A, Record E, Lombard V, Kumar R, Levasseur A, Henrissat B, and Garron ML. (2019) Trichoderma reesei Dehydrogenase, a Pyrroloquinoline Quinone-Dependent Member of Auxiliary Activity Family 12 of the Carbohydrate-Active Enzymes Database: Functional and Structural Characterization. Appl Environ Microbiol. 85. DOI:10.1128/AEM.00964-19 | PubMed ID:31604773 | HubMed [Turbe-Doan2019]
  2. Henrissat B and Garron ML. (2017) How a Glycoside Hydrolase Recognizes a Helical Polyglucan. Structure. 25, 1319-1321. DOI:10.1016/j.str.2017.08.004 | PubMed ID:28877502 | HubMed [Henrissat2017]
  3. Ulaganathan T, Shi R, Yao D, Gu RX, Garron ML, Cherney M, Tieleman DP, Sterner E, Li G, Li L, Linhardt RJ, and Cygler M. (2017) Conformational flexibility of PL12 family heparinases: structure and substrate specificity of heparinase III from Bacteroides thetaiotaomicron (BT4657). Glycobiology. 27, 176-187. DOI:10.1093/glycob/cww096 | PubMed ID:27621378 | HubMed [Ulaganathan2017]
  4. Lafond M, Sulzenbacher G, Freyd T, Henrissat B, Berrin JG, and Garron ML. (2016) The Quaternary Structure of a Glycoside Hydrolase Dictates Specificity toward β-Glucans. J Biol Chem. 291, 7183-94. DOI:10.1074/jbc.M115.695999 | PubMed ID:26755730 | HubMed [Lafond2016]
  5. Shaya D, Zhao W, Garron ML, Xiao Z, Cui Q, Zhang Z, Sulea T, Linhardt RJ, and Cygler M. (2010) Catalytic mechanism of heparinase II investigated by site-directed mutagenesis and the crystal structure with its substrate. J Biol Chem. 285, 20051-61. DOI:10.1074/jbc.M110.101071 | PubMed ID:20404324 | HubMed [Shaya2010]
  6. Zhao W, Garron ML, Yang B, Xiao Z, Esko JD, Cygler M, and Linhardt RJ. (2011) Asparagine 405 of heparin lyase II prevents the cleavage of glycosidic linkages proximate to a 3-O-sulfoglucosamine residue. FEBS Lett. 585, 2461-6. DOI:10.1016/j.febslet.2011.06.023 | PubMed ID:21741976 | HubMed [Zhao2011]
  7. Han YH, Garron ML, Kim HY, Kim WS, Zhang Z, Ryu KS, Shaya D, Xiao Z, Cheong C, Kim YS, Linhardt RJ, Jeon YH, and Cygler M. (2009) Structural snapshots of heparin depolymerization by heparin lyase I. J Biol Chem. 284, 34019-27. DOI:10.1074/jbc.M109.025338 | PubMed ID:19801541 | HubMed [Han2009]
  8. Xiao Z, Bergeron H, Grosse S, Beauchemin M, Garron ML, Shaya D, Sulea T, Cygler M, and Lau PC. (2008) Improvement of the thermostability and activity of a pectate lyase by single amino acid substitutions, using a strategy based on melting-temperature-guided sequence alignment. Appl Environ Microbiol. 74, 1183-9. DOI:10.1128/AEM.02220-07 | PubMed ID:18156340 | HubMed [Xiao2008]
All Medline abstracts: PubMed | HubMed